{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T18:37:30Z","timestamp":1788201450965,"version":"build-2803163510"},"reference-count":74,"publisher":"American Society for Clinical Investigation","issue":"17","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Intramural Research Program of the National Institutes of Health","award":["Z01 AI000949-02 LIG"],"award-info":[{"award-number":["Z01 AI000949-02 LIG"]}]},{"name":"NIAID\/NIH","award":["R01 AI135049"],"award-info":[{"award-number":["R01 AI135049"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,1]]},"abstract":"<jats:p>\n                    Allergen-specific monoclonal antibodies (mAbs) that block IgE binding to allergens are emerging as new therapeutics for treating allergies to pollen, peanuts, and cats. Alpha-Gal syndrome (AGS) is an allergy to galactose-\u03b1-1,3-Galactose (\u03b1-Gal), which is present in mammalian meat and tissue-derived products. Initially aiming to identify mAbs targeting \u03b1-Gal on malaria parasites, we isolated 42 \u03b1-Gal\u2013specific mAbs from B cells of individuals who had been exposed to malaria but found that they bound weakly to the\n                    <jats:italic>Plasmodium falciparum<\/jats:italic>\n                    parasite. These mAbs predominantly used the\n                    <jats:italic>IGHV3<\/jats:italic>\n                    gene family and had a wide range of mutation frequencies. We then screened these mAbs for their ability to bind \u03b1-Gal on AGS allergens and to block the binding of serum IgE of patients with AGS to AGS allergens. Thirteen mAbs bound to the AGS allergens angiotensin-I-converting enzyme (ACE), aminopeptidase-N (AP-N), and cetuximab, and 2 mAbs\u2014 AG028 as both IgA\n                    <jats:sub>2<\/jats:sub>\n                    and IgM, and AG050 IgA\n                    <jats:sub>1<\/jats:sub>\n                    \u2014 blocked the binding of serum IgE from patients with AGS to ACE and AP-N. Additionally, AG028 IgA\n                    <jats:sub>2<\/jats:sub>\n                    and AG028 IgM suppressed ACE-mediated activation of basophils sensitized with serum of patients with AGS. This study supports the development of \u03b1-Gal\u2013specific mAbs as a new intervention to prevent \u03b1-Gal allergy.\n                  <\/jats:p>","DOI":"10.1172\/jci192370","type":"journal-article","created":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T18:01:07Z","timestamp":1788199267000},"source":"Crossref","is-referenced-by-count":0,"title":["Human monoclonal antibodies targeting \u03b1-Gal restrict IgE engagement of \u03b1-Gal syndrome allergens"],"prefix":"10.1172","volume":"136","author":[{"given":"Hyeseon","family":"Cho","sequence":"first","affiliation":[{"name":"Malaria Infection Biology and Immunity Section, Laboratory of Immunogenetics, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, NIH, Rockville, Maryland, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Youngsil","family":"Seo","sequence":"additional","affiliation":[{"name":"Malaria Infection Biology and Immunity Section, Laboratory of 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